ATG9_PODAS
ID ATG9_PODAS Reviewed; 900 AA.
AC Q875A7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Autophagy-related protein 9;
GN Name=ATG9; ORFNames=Pa5D0022;
OS Podospora anserina (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora.
OX NCBI_TaxID=2587412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=s;
RX PubMed=12892638; DOI=10.1016/s1087-1845(03)00025-2;
RA Silar P., Barreau C., Debuchy R., Kicka S., Turcq B., Sainsard-Chanet A.,
RA Sellem C.H., Billault A., Cattolico L., Duprat S., Weissenbach J.;
RT "Characterization of the genomic organization of the region bordering the
RT centromere of chromosome V of Podospora anserina by direct sequencing.";
RL Fungal Genet. Biol. 39:250-263(2003).
CC -!- FUNCTION: Phospholipid scramblase involved in autophagy and cytoplasm
CC to vacuole transport (Cvt) vesicle formation. Cycles between the
CC preautophagosomal structure/phagophore assembly site (PAS) and the
CC cytoplasmic vesicle pool and supplies membrane for the growing
CC autophagosome. Lipid scramblase activity plays a key role in
CC preautophagosomal structure/phagophore assembly by distributing the
CC phospholipids that arrive through ATG2 from the cytoplasmic to the
CC luminal leaflet of the bilayer, thereby driving autophagosomal membrane
CC expansion. Required for mitophagy. Also involved in endoplasmic
CC reticulum-specific autophagic process and is essential for the survival
CC of cells subjected to severe ER stress. Different machineries are
CC required for anterograde trafficking to the PAS during either the Cvt
CC pathway or bulk autophagy and for retrograde trafficking.
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-
CC sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663,
CC ChEBI:CHEBI:57262; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-
CC 3-phosphate)(out); Xref=Rhea:RHEA:67920, ChEBI:CHEBI:58088;
CC Evidence={ECO:0000250|UniProtKB:Q12142};
CC -!- SUBUNIT: Homotrimer; forms a homotrimer with a central pore that forms
CC a path between the two membrane leaflets.
CC {ECO:0000250|UniProtKB:O74312}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q12142}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q12142}.
CC -!- DOMAIN: Forms a homotrimer with a solvated central pore, which is
CC connected laterally to the cytosol through the cavity within each
CC protomer. Acts as a lipid scramblase that uses its central pore to
CC function: the central pore opens laterally to accommodate lipid
CC headgroups, thereby enabling lipid flipping and redistribution of
CC lipids added to the outer leaflet of ATG9-containing vesicles, thereby
CC enabling growth into autophagosomes. {ECO:0000250|UniProtKB:O74312}.
CC -!- PTM: Phosphorylated by ATG1. ATG1 phosphorylation is required for
CC preautophagosome elongation. {ECO:0000250|UniProtKB:Q12142}.
CC -!- SIMILARITY: Belongs to the ATG9 family. {ECO:0000305}.
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DR EMBL; BX088700; CAD60709.1; -; Genomic_DNA.
DR AlphaFoldDB; Q875A7; -.
DR SMR; Q875A7; -.
DR PRIDE; Q875A7; -.
DR VEuPathDB; FungiDB:PODANS_5_5550; -.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR InterPro; IPR007241; Autophagy-rel_prot_9.
DR PANTHER; PTHR13038; PTHR13038; 1.
DR Pfam; PF04109; ATG9; 1.
PE 3: Inferred from homology;
KW Autophagy; Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus;
KW Lipid transport; Membrane; Phosphoprotein; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..900
FT /note="Autophagy-related protein 9"
FT /id="PRO_0000119836"
FT TOPO_DOM 1..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..262
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..434
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 435..455
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 456..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 546..551
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..618
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT INTRAMEM 619..639
FT /evidence="ECO:0000250|UniProtKB:O74312"
FT TOPO_DOM 640..900
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 111..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 900 AA; 102673 MW; 58CBB46E94219B68 CRC64;
MPRKLFSKMP TTQGRSFYEE LRGHDSEGYD GGSRAGLLDE ENLNHNFQDY DLDHAEGLTV
DDSRATLAGL RKTPASKVPP GHQNDRSMWL AHDDDADNDV PPSLLVEPRG AHLAGKPKRK
QSRQAAYTMP GSSNTRAQWE TIQAHQPLHN DEPFTQSHRG NGAPGSLFSG SASLDAKKMA
EWRWANVQNL DKFIKEVYDY YRGCGIKAII TERVLHLGNV AFIAVLLTFL TQCVDYSLVR
GSQKLSQIIV PQCTRKMSGW WNLGLWLFAF YFIWKAIQYI LDLHRLFHVR DFYTHLLNIP
DHDMQTITWQ EVVARVMALR NQNSKTATTL TPLQRHFIGS QSKERLDASD IANRIMRREN
YLIALFNKDI LDLTIPLPFL RNRQYFSRTL EWTLMFSVLD MVFDEKGQVN QKFLRADRRG
EISEKLRSRF QFAGIMILVL SPFVSLYLVI YYFLMYYHEI QKNPSVLSSR SYTPLAEWKF
REFNELPHLF QKRLDMSKAF ATHYMDQFPK VKTEMVAKSV AFVSGALATV LAIASVFDPE
LFLGFEITPD RTVLFYTAIF GSIWAVAHGM QSQDDVVFDP EYAMRNVIEY THYEPDHWKD
RLHSYDIKLE FAELYKPKIV IFLEEILGIL TTPFVLFFSL PKCSDQIIDF FREFTLHIDG
LGYVCTFAEF DFKKAMANAK KPSDGGDVRD EYYSAKHGKM EASYYGFIGN YGNFALNPKG
APGSHLPPGM RNQFHPPPAW PGLNSPPLGA DMQTSRMGRS EFRSRSRAPG QGLRPGPSMV
APSPMASILL DPHHLPPSHL VNPGRASHPH RVQQNRRPGE SNIIEESLED EERGREGVNR
HDDEEVYGHG DGMDESAWQT SPARTLSRDN SAIEGTGTAE AGVVDMIYQF NQAQFTRNGV
